› 6dqo

X-ray diffraction
1.7Å resolution

Crystal structure of SsuE FMN reductase Y118A mutant in FMN bound form.

Released:
DOI: 10.2210/pdb6dqo/pdb
PDB entry 6dqo coloured by chain, front view.
PDB entry 6dqo coloured by chain, side view.
PDB entry 6dqo coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Not as easy as π: An insertional residue does not explain the π-helix gain-of-function in two-component FMN reductases.
McFarlane JS, Hagen RA, Chilton AS, Forbes DL, Lamb AL, Ellis HR
Protein Sci 28 123-134 (2019)
PMID: 30171650

Function and Biology Details

Reaction catalysed: 
FMNH(2) + NADP(+) = FMN + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FMN reductase (NADPH) Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.19 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P80644 (Residues: 1-191; Coverage: 100%)
Gene names: JW0920, b0937, ssuE, ycbP
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: C2221
Unit cell:
a: 80.911Å b: 110.847Å c: 41.727Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.207
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The role of π-helices in TRP channel gating.
Zubcevic et al. (2019)